Oxidation of tyrosine to dopachrome by peroxidase isolated from murine melanoma.

Abstract

Peroxidase, isolated from B16 mouse melanoma, converted tyrosine to dopachrome in the presence of either dopa or dihydroxyfumarate co-factor. A suspended homogenate of cloned, cultured B16 mouse melanoma cells also showed peroxidatic conversion of tyrosine to dopachrome in the presence of dihydroxyfumarate co-factor. The findings confirm previous histochemical, autoradiographic-histochemical, and EM-histochemical studies showing that melanoma peroxidase can convert tyrosine to melanin.

• Authors: M R Okun, L Schley, R Ziegelstein, H Blair
• Journal: Physiological chemistry and physics (Physiol Chem Phys) Vol. 14 Issue 1 Pg. 8-12 ( 1982) ISSN: 0031-9325 [Print] United States
• PMID: 6294694 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't, Research Support, U.S. Gov't, P.H.S.)

Chemical References

• Indolequinones
• Indoles
• Isoenzymes
• Melanins
• Quinones
• dopachrome
• Tyrosine
• Peroxidases
• Peroxidase

Topics

• Animals
• Clone Cells (metabolism)
• In Vitro Techniques
• Indolequinones
• Indoles (metabolism)
• Isoenzymes (metabolism)
• Melanins (biosynthesis)
• Melanoma (metabolism)
• Mice
• Mice, Inbred C57BL
• Neoplasms, Experimental (metabolism)
• Peroxidase
• Peroxidases (metabolism)
• Quinones (metabolism)
• Tyrosine (metabolism)